ID A0A2K6RY09_SAIBB Unreviewed; 510 AA.
AC A0A2K6RY09;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN Name=USP49 {ECO:0000313|Ensembl:ENSSBOP00000000023.1};
OS Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000000023.1, ECO:0000313|Proteomes:UP000233220};
RN [1] {ECO:0000313|Ensembl:ENSSBOP00000000023.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin
CC from specific proteins to regulate different cellular processes.
CC {ECO:0000256|RuleBase:RU366025}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12; Evidence={ECO:0000256|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|RuleBase:RU366025}.
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DR AlphaFoldDB; A0A2K6RY09; -.
DR STRING; 39432.ENSSBOP00000000023; -.
DR Ensembl; ENSSBOT00000000064.1; ENSSBOP00000000023.1; ENSSBOG00000000054.1.
DR GeneTree; ENSGT00940000157997; -.
DR OMA; AWACLKC; -.
DR Proteomes; UP000233220; Unplaced.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:Ensembl.
DR GO; GO:0042393; F:histone binding; IEA:Ensembl.
DR GO; GO:0140936; F:histone H2B deubiquitinase activity; IEA:Ensembl.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF7; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 49; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU366025};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000233220};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 75..479
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 115..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 510 AA; 58113 MW; 6754707A6E3ADDD4 CRC64;
GLSKCWDYRR EPLPGHGGMY LWSHAPPRKS ARLLLHAPRD AGPAATRSTA FPTSRRAPAA
ALKLRRQPAV APGVTGLRNL GNTCYMNSIL QVLSHLQKFR ECFLNLDPSK TEHLFPKATN
GKTQLSGKPT SSSATELSLR SDRAEVCERE GFCWNSGASI SRSLELIQNK EPSSKHISLC
RELHTLFRVM WSGKWALVSP FAMLHSVWSL IPAFRGYDQQ DAQEFLCELL HKVQQELESE
GTTRRILIPF SQRKLTKQVL KVVNTIFHGQ LLSQVTCISC NYKSNTIEPF WDLSLEFPER
YHCIEKGFVP LNQTECLLTE MLAKFTETEA LEGRIYACDQ CNSKRRKSNP KPLVLSEARK
QLMIYRLPQV LRLHLKRFRW SGRNHREKIG VHVVFDQVLT MEPYCCRDML SSLDKETFAY
DLSAVVMHHG KGFGSGHYTA YCYNTEGGFW VHCNDSKLNV CSVEEVCKTQ AYILFYTQRT
VQGNARISET HLQSQVQSSN NDEGRPQTFS
//
